Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo

The overarching goal of this study was to test the hypothesis that curcumin (and other similar  polar Aβ binding compounds) might be able to cross the blood-brain barrier, bind to Aβ and related aggregates, and inhibit beta amyloid fibril formation and beta amyloid plaque deposition.  In these studies the authors used an in vitro model of Aβ fibrillization to show that curcumin can bind amyloid to inhibit Aβ aggregation as well as fibril and oligomer formation with dosing at achievable levels.  In addition the authors demonstrated that curcumin can label plaques in vitro and in vivo, block toxicity of oligomers in vitro, and significantly reduce amyloid levels in aged Tg2576 mice (22 months old) fed a curcumin diet beginning at 17 months after established amyloid deposition. These data suggest that low dose curcumin effectively disaggregates Abeta as well as prevents fibril and oligomer formation and support the rationale for curcumin use in clinical trials preventing or treating AD.